JP3344584B2 - 組換えライブラリースクリーニング法 - Google Patents

組換えライブラリースクリーニング法

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Publication number
JP3344584B2
JP3344584B2 JP50889691A JP50889691A JP3344584B2 JP 3344584 B2 JP3344584 B2 JP 3344584B2 JP 50889691 A JP50889691 A JP 50889691A JP 50889691 A JP50889691 A JP 50889691A JP 3344584 B2 JP3344584 B2 JP 3344584B2
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antibody
protein
bacteriophage
phage
encoding
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JPH05506782A (ja
Inventor
ジェイ． ダウアー，ウィリアム
イー． クウィーラ，スティーブン
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アフィマックス テクノロジーズ ナームロゼ ベノートスハップ
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    • C—CHEMISTRY; METALLURGY
    • C40—COMBINATORIAL TECHNOLOGY
    • C40B—COMBINATORIAL CHEMISTRY; LIBRARIES, e.g. CHEMICAL LIBRARIES
    • C40B40/00—Libraries per se, e.g. arrays, mixtures
    • C40B40/02—Libraries contained in or displayed by microorganisms, e.g. bacteria or animal cells; Libraries contained in or displayed by vectors, e.g. plasmids; Libraries containing only microorganisms or vectors
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
    • C07K16/005—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies constructed by phage libraries
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
    • C12N15/09—Recombinant DNA-technology
    • C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
    • C12N15/1034—Isolating an individual clone by screening libraries
    • C12N15/1037—Screening libraries presented on the surface of microorganisms, e.g. phage display, E. coli display

Description

【発明の詳細な説明】 発明の分野 本発明は一般に組換えDNA技術に関し、より詳しく
は、着目のタンパク質をコードするDNA配列についてDNA
ライブラリーをスクリーニングする方法に関する。
発明の背景 所望のタンパク質をコードする遺伝子を組換えDNAラ
イブラリーから単離することは困難な作業であることが
ある。ハイブリダイゼーションプローブはその工程を促
進することができるが、それらの使用は該タンパク質を
コードする遺伝子の配列の少なくとも一部分が既知であ
ることに依存する。配列が既知でない場合、発現ベクタ
ー中でDNAライブラリーを発現せしめ、そして抗体を使
って所望のタンパク質抗原についてプラークまたはコロ
ニーをスクリーニングしている。この手順は、少数のラ
イブラリーをスクリーニングするのには有用であるが、
105クローン中約１未満において提示される配列は見落
としやすく、106以上のライブラリーをスクリーニング
するのは困難である。
抗体分子は軽鎖と重鎖のポリペプチド鎖から成り、各
々別個の可変（Ｖ）領域を有し、それらが組み合わさっ
て抗原結合領域を形成する。いずれか１つの抗体産生細
胞における重鎖と軽鎖の無作為組合せ事象に基づくと、
抗体の重鎖と軽鎖の可能な組合せレパートリーは1012ま
たはそれ以上の多数であることができる。よって、この
レパートリーの大部分をサンプリングしそして所望の抗
原結合特異性を有する抗体を発現するクローンを得るた
めには、非常に多数のライブラリーを作製しスクリーニ
ングしなければならないだろう。
Huse W.D.他（1989）Science 146:1275−1281はλフ
ァージ中での抗体重鎖および軽鎖のクローニング用ライ
ブラリーの調製を報告している。抗体鎖は、ファージ粒
子の形成とは独立して大腸菌（E.coli）宿主の中で細胞
内的に会合する。
Parmley S.F.＆ Smith G.P.（1988）Gene 73:305−31
8は、融合ファージ上への一本鎖ペプチドの表示および
スクリーニングを教示している。
着目のタンパク質、特に抗体分子をコードするDNA配
列を一層容易に同定し、再クローニングしそして発現せ
しめることができる、スクリーニング工程を容易にする
方法が必要とされている。そのような方法が利用可能と
なれば、動物の全抗体レパートリーを探査すること、例
えば、所定の標的分子に対する抗体を獲得することが可
能になるであろう。こうして、起源の種にかかわらず、
従来のハイブリダイゼーションまたはリンパ芽球様細胞
の形質転換によりモノクローナル抗体を産生する労働集
約的な方法および難点を回避することができる。全く驚
くべきことに、本発明はそれらの要求や他の関連する要
求を満たす。
発明の詳細な説明 本発明は、多重鎖タンパク質を表示するためのバクテ
リオファージの使用であって、前記多重鎖タンパク質の
第一鎖が前記バクテリオファージの外面上のコートペプ
チド（外皮ペプチド）に融合せしめられ、そして前記多
重鎖タンパク質の第二鎖が第一鎖と複合体形成されるバ
クテリオファージの使用を提供する。
本発明はまた、第一ポリペプチド鎖と第二ポリペプチ
ド鎖を含んで成る多重鎖タンパク質をコードするヌクレ
オチド配列についてDNAライブラリーをスクリーニング
する方法であって、前記多重鎖タンパク質はリガンドに
特異的に結合し、 次のヌクレオチド配列メンバー： （ｉ） バクテリオファージのコートペプチドをコード
する配列に融合した第一鎖をコードする、該ライブラリ
ーの第一ヌクレオチド配列メンバー；および （ii） 第二鎖の周縁質分泌を指令するシグナルペプチ
ドをコードする配列に融合した第二鎖をコードする、該
ライブラリーの第二ヌクレオチド配列メンバー を用いて、宿主細胞のバクテリオファージ発現ベクター
形質転換を行い； バクテリオファージ粒子と多重鎖タンパク質の発現お
よび集成に適当な条件下で前記形質転換された細胞を培
養し、ここで前記多重鎖タンパク質はバクテリオファー
ジ粒子の外面上に表示され、所望によりDNAライブラリ
ー配列メンバーの発現が誘導性発現であり、前記DNAラ
イブラリー配列の発現の誘導が、好ましくは少なくとも
１個の完全なバクテリオファージ粒子の集成が起こるま
で遅らされ； 前記多重鎖タンパク質をコードするバクテリオファー
ジを前記リガンドによって選択し、そして 所望であれば、選択されたバクテリオファージ粒子か
ら多重鎖タンパク質の第一鎖と第二鎖をコードするヌク
レオチド配列を単離する段階を更に含んで成り；場合に
より前記バクテリオファージが選択段階の前に宿主細胞
培養物から収得される というスクリーニング方法を提供する。
従って、この方法は、着目のタンパク質をコードする
ヌクレオチド配列についてDNAライブラリーをスクリー
ニングすることに備える。この方法は一般に、着目のタ
ンパク質を、生物学的に活性な形（通常は結合活性を有
する形）において、該タンパク質をコードする特定のDN
A配列に物理的に結び付ける（関連させる）ことを含
む。これは、着目のタンパク質の結合活性に頼るアフィ
ニティー技術による前記DNAの単離および同定を可能に
する。
従って、第二のおよび任意のそれ以降のタンパク質鎖
は細胞周辺腔へと運ばれるようにファージゲノムから発
現され、そこでそれらはファージコートタンパク質に融
合せしめられた第一鎖と結合し、その複合体はそれが細
胞から出ると同時にファージ粒子と会合する。
着目のタンパク質をコードする粒子は適当なアフィニ
ティー富化技術によって培養物から選択することができ
る。これは、着目のタンパク質に特異的なリガンド、例
えば着目のタンパク質が抗体であるならば抗原を使って
達成される。アフィニティー選択手順を繰り返すことに
より、所望の配列をコードするクローンの富化を提供
し、次いで該クローンを配列決定、更なるクローニング
および／または発現のために単離することができる。
ファージは繊維状ファージ、例えばfd,f1またはM13で
あることができる。典型的には、ファージコートタンパ
ク質、例えばp IIIをコードする遺伝子の５′領域にDNA
ライブラリー配列が挿入される。例えば、DNAライブラ
リーメンバーによってコードされるタンパク質に融合し
たファージコートタンパク質が生産され、そしてウイル
ス粒子へと組み立てられる。
シグナル配列はOmp A,pelB,phoA,p IIIまたはβ−ラ
クタマーゼシグナル配列であることができる。
形質転換された宿主細胞を培養後に溶解せしめ、そし
てバクテリオファージ粒子を細胞破片から選択し、所望
によりその選択段階を少なくとも１回繰り返すことによ
り着目のタンパク質をコードするバクテリオファージ粒
子を富化することができる。
好ましい多重鎖タンパク質は抗体またはそれの結合性
断片、好ましくはFab断片である。
ライブラリーの前記第一ヌクレオチド配列メンバー
は、抗体重鎖可変領域を含んで成るタンパク質をコード
することができ、所望により前記抗体重鎖可変領域は前
記バクテリオファージ表面上の前記コートタンパク質の
アミノ末端に置かれる。
第一および第二のDNAライブラリーメンバーは、好ま
しくは増幅されたcDNAを含んで成る。
本発明の方法は、前記多重鎖タンパク質を治療用、予
防用または診断用組成物中に配合する段階を更に含んで
もよい。
従って、本発明により、組換え生産された所望のタン
パク質のクローンを便利に同定するための方法および組
成物が提供される。アフィニティー富化方法は、所望の
リガンド特異性を有するクローンを同定するためのライ
ブラリーのスクリーニングを考慮した方法であり、約10
9までまたはそれ以上の数のクローンを容易にスクリー
ニングすることができる。これは従来技術を上回る有意
な改良を意味する。従来の方法では、典型的には１つの
DNAライブラリーにおいて約106個のクローン、時には10
7個までのクローンのスクリーニングが可能であるが、
時間と労力の比例的増加を伴う。
本発明は、所望の多重鎖タンパク質（例えば抗体分
子）を、それをコードするDNAに物理的に結び付ける
（連関させる）ことを可能にする。次いで、例えばアフ
ィニティー技術によって該タンパク質を富化せしめるこ
とにより、該タンパク質をコードするDNAも富化せし
め、そしてDNAを単離することができる。こうして得ら
れたDNAを別の系においてクローニングし発現させて潜
在的に多量の所望のタンパク質を生産せしめるか、また
は発現前に配列決定および更なるクローニングおよび遺
伝子操作にかけることもできる。
本発明に従ってDNAが富化されクローニングされるタ
ンパク質は、典型的には抗体またはその断片であるが、
ヌクレオチドライブラリーからクローニングすることの
できるどんな多重鎖タンパク質であってもよい。抗体に
加えて、そのようなタンパク質の例としては、例えば、
成長ホルモン、インターフェロン、インターロイキン、
ホルモン、酵素、チモーゲン、等が挙げられる。クロー
ニングすることができるタンパク質は、特異的結合相手
（例えば所望のタンパク質が抗体である時は抗原または
ハプテン）が同定されているものである。
着目のタンパク質が所望の結合特異性の抗体である
時、抗体は特定の種について任意の既知のイソタイプま
たはサブクラスのものであることができ、更に一本鎖も
しくは二本鎖結合複合体またはその部分であることがで
きる。例えば、重鎖の可変抗原結合領域（VH）および／
または軽鎖の可変抗原結合領域（VL）のみを同定し、ク
ローニングすることができる。それによりコードされる
結合性断片（Fv）またはFabは、重鎖もしくは軽鎖の定
常領域に連結されてまたは所望のエフェクター機能を有
する他のタンパク質に連結されて、結合性断片として用
いることができる。定常領域ドメインの特性は、抗体に
予期される用途、例えば診断および／または治療用途、
触媒抗体、等に大部分依存するだろう。
典型的には、タンパク質の結合相手、例えばタンパク
質が抗体である時には抗原またはハプテン、は既知であ
り、本発明の方法は着目の結合相手を特異的に結合する
タンパク質（および該タンパク質をコードするDNA）を
作製および／または同定する手段を提供する。該タンパ
ク質が抗体である時、本発明は、予め決められた抗原ま
たは抗原決定基に対する抗体、特にモノクローナル抗体
を生産するための新規手段を提供し、それによって従来
のモノクローナル抗体技術の面倒で、時間がかかり、し
ばしば予想不可能な方法を回避する。マウスモノクロー
ナル抗体産生は比較的回りくどくないけれども、それは
労働集約的である。更に、従来のアプローチによるヒト
モノクローナル抗体の開発は、様々な技術的難点によっ
て妨害されている。このような難点の大部分は、本発明
によって回避されるだろう。
所望のタンパク質をコードすることができる細胞から
DNAライブラリーが調製される。ライブラリーを調製す
るために様々な技術があり、ゲノムDNAまたはcDNAのい
ずれかより調製することができる。例えば、Sambrook
他,Molecular Cloning,A Laboratory Manual,第２版,Co
ld Spring Harbor Laboratory Press,Cold Spring Harb
or,N.Y.,1989を参照のこと。本明細書中でDNAと呼称す
る時、特記しない限り、DNAはゲノムDNAとcDNAの両者を
包含すると解釈される。RNAまたはDNAの供給源として働
く細胞は、着目のタンパク質をコードすることができる
いずれの細胞でもよい。富化操作および１または複数の
遺伝子を含む領域を増幅するための手段は、既知であれ
ば、使用することができる。例えば、所望のタンパク質
が抗体である時、例えば、非免疫処置動物の脾細胞また
は着目の抗原もしくはハプテンで免疫処置された動物の
脾細胞から、ハイブリドーマ細胞から、あるいはリンパ
芽球様細胞から、調製することができる。非免疫処置動
物の脾細胞の使用は、可能な抗体レパートリーのより好
ましい提示を与え、一方免疫処置動物の脾細胞は免疫処
置用抗原またはハプテンのエピトープに対して向けられ
る配列が富化される。細胞は様々な動物種、例えばヒ
ト、マウス、ラット、ウサギ、ヤギ、ウシ、トリ等から
得ることができ、その選択は着目のタンパク質および意
図する使用目的にしばしば依存する。
着目の細胞、例えば脾細胞またはハイブリドーマ細胞
から単離されたメッセンジャーRNA（mRNA）を表す配列
の増幅は、例えば、米国特許第4,683,202号;Orlandi
他、Proc.Natl.Acad.Sci.USA 86:3833−3837（1989）;S
astry他、Proc.Natl.Acad.Sci.USA 86:5728−5732（198
9）；およびHuse他、Science 246:1275−1281（1989）
において概説されたプロトコールに従って実施すること
ができる。増幅プロトコールにおいて有用であるオリゴ
ヌクレオチドプライマーは、ユニークもしくは縮重であ
るか、または縮重位置にイノシンを含むことができる。
多重鎖免疫グロブリンの場合、通常、重鎖と軽鎖の両方
の可変領域をコードする配列の増幅にプライマーが使わ
れている。予め決められた読み枠における発現用ベクタ
ー中への増幅断片のクローニングを考慮して、制限エン
ドヌクレアーゼ認識配列をプライマーに含めることもで
きる。
増幅されたcDNAを含む発現ライブラリーは、典型的に
はバクテリオファージのようなベクター中で作製され
る。適当なバクテリオファージの特性は使用する特定の
実施態様に依存し、そして通常は、便利には試験管内パ
ッケージングまたは遺伝子形質転換による宿主細胞中へ
の組換えDNAの挿入を可能にし、所望のタンパク質を発
現することができる宿主細胞に感染するものであり、そ
してそのDNAはクローニングに有用な制限部位を含み、
該制限部位は外来DNAの挿入が実質的にファージの本質
的機能を破壊しないであろうファージゲノムの領域中に
置かれる。
上述したように、ライブラリー増幅生成物を効率的に
クローニングできるようにベクターを操作することがで
きる。例えば、オリゴヌクレオチドを用いて、非対称型
制限部位、クローン化配列の発現に最適な距離のところ
にリボソーム結合部位、およびライブラリー増幅生成物
のためのクローニング部位を導入することができる。
所望のタンパク質をコードするクローン化ライブラリ
ー配列を含むファージを富化しそして単離するため、か
くして最終的には核酸配列それ自体を単離するため、細
菌破片から収得したファージがアフィニティー精製され
る。このアフィニティー精製において、所望のクローン
化ライブラリータンパク質に特異的なリガンドまたは結
合相手が使われる。例えば、所望のタンパク質が特定の
抗原または抗原決定基を特異的に結合する抗体である
時、そのような抗原または抗原決定基を使って、外面上
に所望のタンパク質を有するファージまたは外面の一部
分を捕捉する。リガンドは、典型的には不溶性支持体、
例えば粒子またはビーズまたはプレートに吸着される。
こうして得られたファージは、次いで宿主細胞中に感染
せしめることによって増幅させることができる。所望の
富化レベルに達するまでまたはバックグラウンドファー
ジに対して標的ファージがもはや富化されなくなるま
で、一回あたり104倍ほどまたはそれより大きいアフィ
ニティー富化の繰り返し、および増幅を使うことができ
る。
富化された抗体−ファージは、同一のまたは別の結合
相手をプローブとして使う追加の検出技術、例えば発現
プラーク（またはコロニー）リフト〔例えば、Youngお
よびDavis,Science 222:778−782（1983）を参照のこ
と〕を使ってスクリーニングすることもできる。スクリ
ーニングは追加のアッセイ（例えば触媒活性についての
アッセイ）を用いることもあり、該アッセイは、所望の
性質を有するタンパク質を発現するプラークをその場で
検出するのに使われる。スクリーニングプロトコールか
ら得られたファージを細胞中に感染せしめ、増殖させ、
ファージDNAを単離しそして配列決定し、そして／また
は原核生物もしくは真核生物中での遺伝子発現用ベクタ
ー中に再クローニングし、多量の選択された特定のタン
パク質を得る。
本発明によれば、所望のタンパク質は、ウイルスコー
トタンパク質との融合タンパク質として宿主細胞の細胞
質外区域、例えば細菌の周縁質に輸送される。この態様
では、所望の多重鎖タンパク質（例えば抗体）の１つの
鎖がウイルスコートタンパク質に融合された形で発現さ
れ、それがプロセシングされて細胞内膜に運ばれる。存
在するなら、他の鎖は分泌リーダーを伴って発現され、
かくして同様に周縁質または別の細胞内であるが細胞質
外である場所に運ばれる。細胞質外にある鎖（例えば軽
鎖と重鎖）は次いで完全なタンパク質（またはその結合
性断片）に集成される。集成された分子は、ファージが
宿主の細胞膜から突き出てコートタンパク質がファージ
DNAの周りに集合するにつれて、ファージコートタンパ
ク質への付着によってファージ中に取り込まれるように
なる。
この態様では、cDNAの合成および増幅は上記の通り行
われ、次いでコートタンパク質をコードするベクター配
列の中または付近にクローニングされる。ここで、ベク
ターは、繊維状ファージ、例えばf1,fd,Pf1,M13等であ
るかまたはそれらから誘導される。好ましい態様では、
繊維状ファージはfd−tetである。ファージベクター
は、ファージコートタンパク質、例えばp IIIコートタ
ンパク質をコードする遺伝子の５′領域に置かれたクロ
ーニング部位を含むように選択される。適当なベクター
（例えば下記に記載するfd−tet B1）は、外来配列が成
熟コートタンパク質のＮ末端にまたはその付近に発現さ
れるような外来配列の指向型クローニングを可能にす
る。
ドナー細胞からのcDNA（例えばVH領域）をコートタン
パク質遺伝子（例えば遺伝子III,“g III"）クローニン
グ部位中にクローニングすることにより、ライブラリー
を作製する。クローン化配列、例えばVH領域のクローン
化配列は、最終的には、集成されたファージ粒子の外側
の接近しやすい表面上に、成熟コートタンパク質のＮ末
端に融合したポリペプチドまたはタンパク質（VHタンパ
ク質の場合には約120アミノ酸までの）として発現され
る。コートタンパク質のＮ末端付近の大きなペプチド断
片は、同様に置かれたずっと小さい断片を有するファー
ジと比較して、ファージ感染力および／または収量の減
少を引き起こし得るけれども、大きな断片は本明細書に
記載の方法によって効率的に富化せしめることができ
る。
或るペプチドは、それらのサイズおよび／または配列
のため、それらのキャリヤーファージの感染力の重大な
欠損を引き起こし得る。これは各選別サイクル後の再感
染および増幅の間に集団からのファージの損失を引き起
こす。この欠損性感染力に関連する問題を最小にするた
め、溶出したファージから調製したDNAをエレクトロポ
レーションまたは周知の化学的手段によって宿主細胞中
に形質転換せしめる。マーカー発現に十分な期間に渡り
細胞を培養し、DNA形質転換に典型的に実施される通り
に選別を行う。コロニーを増幅せしめ、次いでその後の
選別工程のために後述のようにしてファージを収得す
る。
所望のタンパク質が多重鎖タンパク質、例えば抗体ま
たはその結合性断片である時、ファージコートタンパク
質中にクローニングされない１または複数の鎖をコード
するcDNAは、第一鎖−コートタンパク質ライブラリーを
含むベクターの適当な部位（後述）中に直接クローニン
グされ；または好ましくは、それ以降の１または複数の
鎖は異なるプラスミドベクター中での別個のライブラリ
ーとしてクローニングされ、増幅され、そして該断片を
第一鎖−コートタンパク質ライブラリーベクター中に取
り付けることができる。例えば、第一鎖が抗体重鎖また
はその結合性断片である時、軽鎖VL cDNA配列の最終目
的地は、コートタンパク質遺伝子中にVH配列を既に含む
ベクターファージRF DNA中であり、これによって単一
ファージゲノム中でVH配列とVL配列を無作為に組み換え
る。
所望の多重鎖タンパク質の第二またはそれ以降の鎖、
例えばVLは、宿主細胞の周縁質へのそれの分泌を指令す
るであろうシグナルペプチドリーダー配列と共に発現さ
れるようにしてクローニングされる。例えば、幾つかの
リーダー配列が大腸菌中で抗体配列の分泌を指令するこ
とが示されている。その例は、OmpA〔Hsiung他、Biotec
hnology 4:991−995（1986）〕、pelB〔Better他、Scie
nce 240:1041−1043（1988）〕、phoA〔SkerraおよびPl
uckthun,Science 240:1038−1043（1988）〕およびβ−
ラクタマーゼ〔Zemel−Dreasen ＆ Zamir,Gene 27:315
−322（1984）〕である。
第二以降の鎖のcDNAのためのクローニング部位は、そ
れが正常なファージ機能を実質的に妨害しないように置
かなければならない。１つのそのような位置は、Zinder
およびBoeke,Gene 19:1−10（1982）により記載された
遺伝子間領域である。VL配列は、VL鎖とVH鎖の効率的な
会合を提供するのに十分に高い周縁質中のVL濃度を維持
するために、好ましくはVH/p III生産物と同じかまたは
それより高いレベルにおいて発現される。
一般に、ファージコートタンパク質、例えば繊維状フ
ァージfdのp IIIを使う好結果のクローニング方法は、
（１）全長の（または全長に近い）コートタンパク質
（例えばp III）のＮ末端に融合されたタンパク質鎖
（または所望のタンパク質が多重鎖である時は第一ポリ
ペプチド鎖、例えばVH鎖）の発現および宿主の内膜への
輸送を提供し、ここでコートタンパク質のＣ末端領域中
の疎水性領域は融合タンパク質を膜内に固定し、第一鎖
を含むＮ末端は細胞周辺腔中に突き出しておりそして第
二鎖またはそれ以降の鎖（例えばFvまたはFab断片を形
成するVL）との相互作用に利用可能であり、こうしてコ
ートタンパク質に結合され；（２）存在するならば第二
のまたはそれ以降のポリペプチド鎖（例えばVL）の適切
な発現および周縁質（ペリプラズム）の可溶性区域への
この鎖の輸送を提供し；そして（３）必ずではないが通
常は、正常なファージ機能または宿主細胞の生存能をほ
とんどまたは全く妨害しないだろう。
重鎖と軽鎖の可能な組合せの数はおそらく1012を越え
るだろう。できるだけ多数の組合せをサンプリングする
ことは、多数の形質転換体を回収できることに一部かか
っている。プラスミド様形態を有するファージ（繊維状
ファージのような）には、電気的形質転換が、非常に高
いDNA挿入容量に加えて、試験管内パッケージングを使
ったλファージ形質転換に匹敵する形質転換効率を提供
する。これによって、非常に多数の形質転換体を得るの
に多量のベクターDNAを使用できるようになる。Dower
他、Nucleic Acids Res.16:6127−6145（1988）により
記載されている方法を使って、連結されたベクター１μ
ｇあたり形質転換体約107個の割合において、fd−tet由
来の組換え体を大腸菌（例えばMC1061株）中に形質転換
せしめることができ、そして約３×108構成員までまた
はそれより多数のfd−tet B1においてライブラリーを作
製することができる。DNA挿入容量を増加させそして当
業者の能力の範囲内でクローニングプロトコールに変更
を行うことにより、形質転換体の回収率の約10倍より大
きな増加を加え、1010までまたはそれより多数の組換え
体のライブラリーを提供することができる。
形質転換体は、適当な抗生物質（fd−tetベクターの
場合はテトラサイクリンである）中での増殖により選択
される。これは固形増殖培地上または液体増殖培地中で
行うことができる。固形培地上での増殖には、例えば、
選択性抗生物質を含むＬ−寒天の大表面上で高密度（約
108〜109tfs/m2）において細胞を増殖せしめて本質的に
周密層を形成させる。細胞と押し出されたファージを表
面から掻き採り、本質的にはParmley ＆ Smith,Gene 7
3:305−318（1988）により記載された通りに第１回目の
選別に向けてファージを調製する。液体培地中での増殖
では、Ｌ−ブロスと抗生物質中で約10回またはそれ以上
の倍々増殖を通して細胞を増殖させることができる。後
述の通りに更に変形された標準手順〔Sambrook他（198
9）Molecular Cloning,第２版，前掲,M13ファージの調
製を参照のこと〕によりファージを収得する。固形培地
上での増殖は増幅工程中の偏りの見込みが少ない一方、
ライブラリーのサイズのため液体培養での増殖の方が便
利なことがある。
所望のクローンのアフィニティー富化のために、約10
3〜104ライブラリー当量（１ライブラリー当量は各組換
え体１つずつである……109構成員を有するライブラリ
ーの104当量は109×104＝1013ファージである）を、所
望のタンパク質（例えば抗体）を捜し出すハプテン（リ
ガンド）と共にインキュベートする。ハプテンはアフィ
ニティー富化方法に適当な複数形態のうちの１つであ
る。一態様では、ハプテンは表面または粒子上に固定化
されており、通常は抗体結合部位と自由な相互作用がで
きるように表面から十分遠く離れてハプテンを保持する
のに十分な長さ（例えば、炭素数３〜12）の鎖により取
り付けられている。次いで、抗体を所有するファージの
ライブラリーは、下記の実施例の項目で記載される方法
に従って、固定化されたハプテン上で選別される。
ハプテン提示の第二の例は、認識可能なリガンドに
（同じく或る長さの鎖によって）取り付けられたハプテ
ンである。そのようなリガンドの特定例はビオチンであ
る。このように修飾されたハプテンをファージのライブ
ラリーと共にインキュベートすると、溶液中で両方の反
応体との結合が起こる。生じた複合体を次いでビオチン
成分を通してストレプトアビジン（またはアビジン）に
結合させる。ストレプトアビジンはプラスチックプレー
トのような表面上または粒子上に固定化することがで
き、この場合、そこに複合体（ファージ−抗体−ハプテ
ン−ビオチン−ストレプトアビジン）が物理的に保持さ
れ；または、ストレプトアビジンを例えば蛍光団によっ
て標識して、例えば蛍光標識細胞選別器上での選別操作
による検出および／または単離のために活性ファージ／
抗体に標識を取り付けることができる。
所望の特異性を持たない抗体を有するファージは、洗
浄によって除去される。要求される洗浄の程度および緊
縮性は着目のタンパク質ごとに決定されるだろう。結合
インキュベーションおよびその後の洗浄の条件を調整す
ることにより、回収される抗体の結合特性に或る程度の
制御を与えることができる。温度、pH、イオン強度、二
価カチオン濃度、並びに洗浄容量および洗浄期間は、ハ
プテンに対して特定範囲内の親和力を有する抗体を得る
ために選択されるだろう。遅い解離速度に基づく選択
（通常、高親和力が予想される）が最も実用的なルート
である。これは、飽和量の遊離ハプテンの存在下での連
結インキュベーションにより、または洗浄の容量、回数
および長さを増加させることにより、行うことができ
る。どちらの場合も、解離された抗体−ファージの再結
合が防止され、そして時間を長くすればするほどますま
す高い親和力の抗体−ファージが回収される。
結合および洗浄操作の追加の変更を適用して、特別な
性質を有する抗体を見つけることができる。ある抗体の
親和力はイオン強度またはカチオン濃度に依存する。こ
れは、抗体からタンパク質を除去するのに穏和な条件が
要求される時、種々のタンパク質のアフィニティー精製
に用いられる抗体にとって有用な性質である。特定例
は、結合活性がCa++に依存する抗体およびEGTAの存在下
でそれらのハプテンを遊離する抗体である。Hopp他、Bi
otechnology 6:1204−1210（1988）を参照のこと。そ
のような抗体は、最初はCa++の存在下でハプテンを結合
するものを単離し、次いでこのグループ中EGTAの存在下
で結合することができないものを同定することによる二
重スクリーニング技術によって、組換え抗体ライブラリ
ー中に同定することができる。
ある種の触媒活性を有する抗体は、反応体（基質およ
び中間体）に対して高い親和力を有する生成物に対して
は低い親和力を有する抗体のグループの中で富化せしめ
ることができる。それらの性質を有する抗体を富化せし
める二重スクリーニング技術は、特定の反応体を触媒す
る抗体を見つけるのに有用である。更に、ある種の開裂
反応を行うことができる触媒抗体を選択することもでき
る。そのような反応体の１つのカテゴリーは、ある分子
からの特定の末端基の開裂である。例えば、ペプチドの
末端から特定のアミノ酸を開裂する触媒抗体は、該ペプ
チドを固定化し、そして結合を促進するが開裂は促進し
ないと予想される条件（末端基および開裂反応の性質に
依存して、例えば低温、特定のイオン強度、pH、カチオ
ン濃度、等）の下で抗体ライブラリーを選別し、次いで
洗浄することによって選択することができる。これは末
端基を認識する抗体を結合させそして固定化された状態
にするので、このグループから開裂を行うことができる
ものが手に入るだろう。開裂を行うことができるものを
見つけるために、開裂に好ましい条件に条件が転換され
る。この段階は、固定化されたペプチドを含まない自分
自身を開裂することができる抗体−ファージを遊離させ
るだろう。
これを達成する別のやり方は、開裂される結合とは異
なる結合（例えば、非ペプチド結合）に末端基を取り付
けることにより、特定の末端基に結合する抗体について
選択を行うことである。次いでその適当な結合を介して
取り付けられた末端基に対して開裂条件下でその後の選
別（第一回目のスクリーニングからの陽性ファージの選
別）を行うことにより、非結合画分において所望の触媒
活性を有するものが富化されるだろう。
固定化されたハプテンから活性抗体−ファージを溶出
せしめるため、適当な緊縮性での洗浄後、結合した（活
性）ファージを、通常はpH変化を使った溶出により回収
する。例えば、pH2またはpH11を使うことができ、次い
でこれを中和し、そして溶出したファージを宿主細胞の
感染または形質転換によって増幅させる。そのような宿
主の例は大腸菌（E.coli）MC1061−F'KANまたはK91であ
る。次いで宿主細胞をテトラサイクリン耐性コロニーと
して増殖させる。該コロニーを掻き採り、コロニーから
押し出されたファージを上記のような標準手順によって
精製する。次いでそれらのファージを別のアフィニティ
ー富化（選別）操作に使用し、所望の富化レベルが達成
されるまでまたはバックグラウンドファージに比較して
標的ファージがもはや富化されなくなるまで、このサイ
クルを繰り返す。繰り返し選別操作およびその間の増幅
は、107倍を越える富化レベルを提供することができ
る。個々のクローンを単離するために、最終回の選別お
よび溶出から得られたファージを用いて細胞を感染せし
めるかまたはそれらのDNAを用いて細胞を形質転換せし
め、寒天（通常はＬ−寒天）および抗生物質（通常はte
t）上で増殖させて十分に分離された個々のコロニーを
形成せしめる。そのコロニーの各々がVH配列とVL配列の
両方を有するファージゲノムを担持しているクローンで
ある。各コロニーから押し出されたファージ粒子から一
本鎖DNAを単離することができ、そしてVHおよびVL断片
をコードするDNAを配列決定することができる。標準法
によりファージDNAの複製可能形態（二本鎖）を単離
し、クローニング部位中のDNA（VHおよびVL配列）を、
原核生物または真核生物中での遺伝子産物の発現用に設
計されたベクター中に再クローニングし、スクリーニン
グ工程で選択された特定の抗体を多量に得ることができ
る。
標的リガンドにより認識される抗体を有すると同定さ
れたファージは、使用する特定のファージベクターに適
当なように増殖される。fd−tetについては、抗生物質
（Tet）選択を有する栄養培地（例えばＬ−ブロス）の
液体培養において行われる。ファージを収得し、DNAを
調製し、標準法によって配列決定し、特定の抗体のDNA
配列とアミノ酸配列を決定する。
該DNAは適当な真核または原核発現ベクター中に再ク
ローニングし、多量のタンパク質の生産のために適当な
宿主中にトランスフェクトせしめることができる。この
発現系から標準手順によって抗体を精製する。抗体の結
合親和力は、Harlow ＆ Lane,Antibodies,A Laboratory
Manual,Cold Spring Harbor,N.Y.（1988）に記載され
たような標的抗原または触媒活性を用いる公知のイムノ
アッセイにより確かめることができる。
下記の実施例は例示の目的で与えられ、限定目的では
ない。
実施例Ｉ この実施例は、予め選ばれた抗原に結合する抗体を単
離し、それによって該抗体をコードするヌクレオチド配
列を単離する手順を記載する。免疫グロブリン発現ライ
ブラリーは、繊維状ファージfdを使ってマウス脾細胞か
ら調製する。抗体重鎖はコートタンパク質p IIIとの融
合タンパク質として発現せしめる。所望の結合特異性の
抗体を含むファージ粒子は、予め選ばれた抗原を使った
選別操作を使って単離する。
ベクターの作製 テトラサイクリン耐性形質導入ベクターfdTet（Zache
r他、1980）から繊維状バクテリオファージベクターfdT
etB1を作製した。fdTetB1中のクローニング部位を遺伝
子IIIのＮ末端領域中に操作し、18塩基対により隔てら
れた２つの非相補的Bst XI部位を含ませた。これは、ま
ずfdTetのTN10領域中に既に存在するBst XI制限部位を
削除することによって行った。RF DNAをBst XI制限エン
ドヌクレアーゼで消化し、次いでT4ポリメラーゼを添加
して突出３′末端を除去した。平滑末端にされた分子を
連結し、MC1061中に電気形質転換せしめた。幾つかのテ
トラサイクリン耐性形質転換体からRF DNAを単離し、Bs
t XI制限エンドヌクレアーゼで消化した。この酵素で消
化されなかったクローンを、オリゴヌクレオチド５′−
TATGAGGTTTTGCCAGACAACTGGAACAGTTTCAGCGGAGTGCCAGTAGA
ATGGAACAACTAAAGG−３′を用いた部位特異的突然変異誘
発〔Kunkel他、Meth.Enzymol.154:367−382（1987）〕
により、クローニング部位の挿入について選択した。幾
つかのテトラサイクリン耐性形質転換体から単離したRF
DNAのジデオキシ配列決定により、正しい変異原性配列
の挿入を確かめた。
縮重オリゴヌクレオチドライブラリーの作製 TN10領域中に一対の非相補的Sfi I部位を含むベクタ
ーfdTetBSNを作製した。この部位は、軽鎖ライブラリー
からの発現カセットの最終挿入目的地である。ユニーク
Hind III部位のところでfdTetB1を開環せしめた。２つ
の相補的合成オリゴヌクレオチドをリン酸化し、アニー
ルさせて次の構造を形成せしめた： このオリゴ体を標準法によりfdTetB1のHind III部位に
連結せしめた。正しく連結され環化された分子は１つも
Hind III部位を含まないので、リガーゼを不活性化した
後、反応物をHind IIIで再切断して挿入断片を取り込ま
なかったプラスミドを線状化した。次いでこの材料を大
腸菌中に形質転換せしめ、テトラサイクリン上で選択し
た。得られた分子の構造を確認し、それらをfdTetBSNと
命名した。
ベクターfdTetSXNSを作製するために、fdTetBSNをBst
XI部位のところで開環せしめ、次の構造を与えるよう
にアニール化されたオリゴヌクレオチド： をfdBSNのBst XI部位に連結せしめ、重鎖断片を収容す
るためのユニークXho IおよびSpe I部位を提供した。
pUC19をAlwN Iで消化しそして末端を平滑にすること
により、プラスミドベクターpVLを作製した。アニール
したオリゴヌクレオチド： を平滑AlwN I部位に連結せしめることにより、Sfi I部
位を導入した。
この変形pUC19のAat II部位を開き、Huse他により記
載された軽鎖発現カセットを含む断片を、下流側（転写
方向に関して）で配列GGCCGGTCCGGCCのSfi I部位により
隣接させた。このプラスミドは、（時計回りの方向で）
Sfi I部位、β−ラクタマーゼ遺伝子、lacZプロモータ
ー、リボソーム結合部位、pel Bシグナルペプチド配
列、Sac I部位、Xba I部位、翻訳終結部位、およびSfi
I部位を含んでいる。
別個の重鎖および軽鎖ライブラリーの作製 抗体重鎖および軽鎖の抗原結合領域を表すcDNAを、Hu
se他（前掲）により記載された方法で抗体産生細胞のRN
Aから合成した。所望の抗体が結合する予め選択された
抗原によって免疫処置されているマウスの脾細胞を使用
した。可変抗原結合領域に隣接する多数の抗体配列に共
通の領域にアニーリングするプライマーを使ったPCRに
より、cDNAを増幅させた。このプライマーは、後述のよ
うな適当な制限部位も含んだ。増幅された二本鎖断片を
適当な制限ヌクレアーゼで消化し、それぞれのベクター
中の適合する部位に連結せしめた。重鎖断片について
は、これは５′−PCRプライマー中へのXho I部位の組み
込みおよび３′−PCRプライマー中へのSpe I部位の組み
込みによって達成された。次いでそれらの部位を消化に
より暴露し、消化されたfdTetSXNSベクター中の対応部
位に連結せしめた。次いで連結生成物を用いてエレクト
ロポレーションにより大腸菌MC1061を形質転換せしめ、
過剰増殖後、アンピシリン上での選択により形質転換体
を選択した。
組合せ重鎖−軽鎖発現ライブラリーの作製 軽鎖ライブラリー（pVL中）からのDNAをSfi Iで消化
した。生じた２断片のうちの大きい方（軽鎖発現カセッ
トを含む）を単離し、Sfi Iで消化された重鎖ライブラ
リー（fdTetSXNS中）のDNAに数倍モル過剰で連結せしめ
た。連結生成物を用いてエレクトロポレーションにより
大腸菌MC1061細胞を形質転換せしめた。一定期間の過剰
増殖後、形質転換体をアンピシリン（100μg/m）とテ
トラサイクリン（20μg/m）上で二重選択した。得ら
れた形質転換体はfdTetSXNS中の軽鎖と重鎖断片の組合
せライブラリーを構成した。
cDNA合成、制限消化、断片のリン酸化および再連結の
方法は、本質的にはSambrookら（前掲）に書かれた通り
である。どの場合でも、形質転換しようとするDNAを0.3
M酢酸ナトリウムの存在下でエタノール沈澱せしめ、水
に再懸濁した。電気形質転換はDower他（前掲）に記載
された通りに行った。SOC培地（２％バクト−トリプト
ン、0.5％バクト−酵母エキス、10mM NaCl、2.5mM KC
l、10mM MgCl2、10mM MgSO4、20mMグルコース）中で37
℃にて１時間の非選択的過剰増殖後、アリコートを取り
出し、幾つかの希釈液を適当な抗生物質（20μg/mの
テトラサイクリン、100μg/mのアンピシリン、または
両方）を含むLBプレート上に塗抹した。形質転換体の残
りを使って適当な抗生物質を含むＬ−ブロス１に接種
し、そして様々な時間増殖させてライブラリーを増幅せ
しめた。この培養物からファージを単離し、４℃で保存
した。
ファージの単離 液体培養物からの精製ファージは、上清を遠心によっ
て２回清澄化し、そしてポリエチレングリコール（最終
濃度3.3％ポリエチレングリコール8000、0.4M NaCl）で
ファージ粒子を沈澱させることにより得られた。遠心
後、ファージペレットをTBS（50mM Tris−HCl,pH7.5,15
0mM NaCl）中に再懸濁し、４℃で保存した。寒天表面か
らコロニーを掻き採り、Ｌ−ブロス中に再懸濁した後、
この方法でプレート保存物からもファージを単離した。
アフィニティー精製 約103〜104ライブラリー当量のファージを４℃におい
て１μｇの精製抗体と一晩反応させた。次のような手順
によって混合物を選別した。まず、60×15mmのポリスチ
レン製ペトリ皿を1mのストレプトアビジン溶液（0.1M
NaHCO3,pH8.6,0.02％ NaN3中、1mg/m）で被覆し、４
℃で一晩インキュベートした。翌日、ストレプトアビジ
ン溶液を除去した。このプレートを10mのブロッキン
グ溶液（0.1M NaHCO3,pH9.2,0.02％ NaN3中の30mg/m
のBSA、３μg/mのストレプトアビジン）で満たし、室
温で２時間インキュベートした。抗体と反応させたファ
ージライブラリーに２μｇのビオチン化ヤギ抗マウスIg
G（BRL）を添加し、４℃で２時間インキュベートした。
選別の直前に、ストレプトアビジン被覆プレートからブ
ロッキング溶液を除去し、プレートをTBS/0.05％ Tween
20で３回洗浄した。次いで、抗体と反応させたファー
ジライブラリーをプレートに添加し、室温で30分間イン
キュベートした。このアフィニティー精製においてスト
レプトアビジン被覆アガロースビーズ（BRL）を使うこ
ともできる。ファージ溶液を除去した後、プレートを60
分間に渡りTBS/0.05％ Tween 20で10回洗浄した。溶出
緩衝液（1mg/m BSA,0.1N HCl,グリシンでpHを2.2に調
整）をペトリ皿に添加しそして10分間インキュベートし
て免疫複合体を解離させることにより、結合したファー
ジを溶出せしめた。溶出液を取り出し、2M Tris（pH未
調整）で中和し、これを使って対数期のＦ′含有細菌細
胞を感染せしめた。それらの感染細胞を、テトラサイク
リン（20μg/m）を含むLB寒天プレート上に塗抹し、3
7℃で一晩増殖させた。上記と同様にプレートからファ
ージを単離し、２〜３回アフィニティー精製工程を繰り
返した。最終回の精製後、溶出液の一部を使って細胞を
感染せしめ、感染細胞をLBテトラサイクリンプレート上
に低密度で塗抹した。2mのLBテトラサイクリンを含む
培養試験管に個々のコロニーを移し、飽和まで増殖させ
た。96ウエルミクロタイタープレートを用いるBeckman
Biomek Workstation用に考案された方法〔Mardis ＆
Roe,Biotechniques 7:840−850（1989）〕を使ってファ
ージDNAを単離した。Sequenase （U.S.Biochemical
s）、およびfdTetB1中の第二のBst XI部位の40ヌクレオ
チド３′側に存在する配列に相補的であるオリゴヌクレ
オチド配列決定用プライマー（5'−CGATCTAAAGTTTTGTCG
TCT−3'）を使って、ジデオキシ法により一本鎖DNAを配
列決定した。
上記から、大規模のDNAライブラリーから着目のタン
パク質、特に抗体、をコードするヌクレオチド配列を単
離する能力を実質的に増加させる組成物および方法が提
供されることは明白である。これは特に、それらの方法
および組成物が、以前には得られるとしても大規模な実
験によってのみ入手可能であった、治療用または予防用
組成物、診断試薬、触媒化合物等として有用な多数のタ
ンパク質、特にモノクローナル抗体、を回収または初め
から生産するのに使用できるという点で励みになる。本
発明は、モノクローナル抗体技術、特にヒトモノクロー
ナル抗体技術の従来法に関連する難点の多くを回避する
手段を提供する。更に、本発明により同定されたタンパ
ク質は組換え手段によって生産され、これは特に、簡便
性、実質的純度および経済性という追加の利点を提供す
る。
理解の明確化のため本発明を今まで説明と実施例によ
って幾分詳細に記載してきたが、添付の請求の範囲から
逸脱することなく幾つかの変更および改良を行い得るこ
とは明らかであろう。
───────────────────────────────────────────────────── フロントページの続き (51)Int.Cl.7 識別記号 ＦＩ Ｃ１２Ｒ 1:92） (56)参考文献 国際公開88／6630（ＷＯ，Ａ１) Ｓｃｉｅｎｃｅ，1989年，Ｖｏｌ. 246，ｐ．1275−1281 Ｓｃｉｅｎｃｅ，1988年，Ｖｏｌ. 240，ｐ．1038−1041 Ｓｃｉｅｎｃｅ，1988年，Ｖｏｌ. 240，ｐ．1041−1043 Ｎａｔｕｒｅ，1984年，Ｖｏｌ．312, ｐ．643−646 (58)調査した分野(Int.Cl.7，ＤＢ名) C12N 15/09 ZNA G01N 33/53 C12N 7/00 C12P 21/08 ＢＩＯＳＩＳ（ＤＩＡＬＯＧ) ＣＡ（ＳＴＮ)

Claims (6)

    (57)【特許請求の範囲】
  1. 【請求項１】一方が重鎖でありそして他方が軽鎖である
    第一ポリペプチド鎖と第二ポリペプチド鎖を含んで成る
    抗体又はその結合性断片をコードするヌクレオチド配列
    についてDNAライブラリーをスクリーニングする方法で
    あって、前記抗体又はその結合性断片は特定のリガンド
    に特異的に結合し、 次のヌクレオチド配列メンバー： （ｉ）バクテリオファージのコートペプチドをコードす
    る配列に融合した前記第一ポリペプチド鎖をコードする
    前記ライブラリーの第一ヌクレオチド配列メンバー；お
    よび （ii）前記第二ポリペプチド鎖の周縁質分泌を指令する
    シグナルペプチドをコードする配列に融合した前記第二
    ポリペプチド鎖をコードする前記ライブラリーの第二ヌ
    クレオチド配列メンバー を用いて宿主細胞のバクテリオファージ発現ベクター形
    質転換を行い； バクテリオファージ粒子と抗体又はその結合性断片の発
    現および集成に適当な条件下で前記形質転換された細胞
    を培養し、ここで前記抗体又はその結合性断片はバクテ
    リオファージ粒子の外面上に表示され；そして 前記抗体又はその結合性断片をコードするバクテリオフ
    ァージを前記リガンドによって選択する 段階を含んで成り、そして所望であれば、選択されたバ
    クテリオファージ粒子から抗体又はその結合性断片の第
    一および第二ポリペプチド鎖をコードするヌクレオチド
    配列を単離する段階を更に含んで成り；場合により前記
    バクテリオファージが選択段階の前に宿主細胞培養物か
    ら収得されることを特徴とする方法。
  2. 【請求項２】前記バクテリオファージ発現ベクターが繊
    維状バクテリオファージである、請求項１に記載の方
    法。
  3. 【請求項３】前記繊維状バクテリオファージがM13,fdま
    たはf1である、請求項２に記載の方法。
  4. 【請求項４】記コートペプチドがp IIIタンパク質であ
    る、請求項１〜３のいずれか一項に記載の方法。
  5. 【請求項５】前記抗体の結合性断片がFab断片である、
    請求項１に記載の方法。
  6. 【請求項６】前記ライブラリーの第一ヌクレオチド配列
    メンバーが抗体重鎖可変領域を含んで成るタンパク質を
    コードし、場合により前記抗体重鎖可変領域が前記バク
    テリオファージ表面上の前記コートペプチドのアミノ末
    端のところに置かれる、請求項１〜５のいずれか１項に
    記載の方法。
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DK0866136T3 (da) 2005-05-17
ATE174067T1 (de) 1998-12-15
EP0527839A4 (en) 1993-06-09
EP1555328A3 (en) 2009-05-06
DK0527839T3 (da) 1999-08-16
AU7793991A (en) 1991-11-27
DE69133437T2 (de) 2006-01-05
JPH05506782A (ja) 1993-10-07
DE98200770T1 (de) 2004-09-30
ES2124224T3 (es) 1999-02-01
ES2235284T3 (es) 2005-07-01
EP0527839A1 (en) 1993-02-24
US5580717A (en) 1996-12-03
EP0866136B1 (en) 2005-01-12
DE69130563T2 (de) 1999-06-24
ATE286985T1 (de) 2005-01-15
DE69130563D1 (de) 1999-01-14

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